期刊
NATURE COMMUNICATIONS
卷 10, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-019-08646-8
关键词
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资金
- DOE Office of Science [DE-SC0012704]
- Cell and Molecular Biology NIH training grant [NIH-5T32GM008136]
- NIH [1R01GM129666]
- Wellcome [208361/Z/17/Z]
- BBSRC [BB/P01948X/1, BB/R002517/1, BB/S003339/1]
- EPSRC [EP/L000253/1]
- BBSRC [BB/R002517/1, BB/S003339/1, BB/P01948X/2, BB/P01948X/1] Funding Source: UKRI
- EPSRC [EP/R029407/1, EP/R004722/1, EP/L000253/1] Funding Source: UKRI
Extracellular glycan biosynthesis is a widespread microbial protection mechanism. In Gram-negative bacteria, the O antigen polysaccharide represents the variable region of outer membrane lipopolysaccharides. Fully assembled lipid-linked O antigens are translocated across the inner membrane by the WzmWzt ABC transporter for ligation to the lipopoly-saccharide core, with the transporter forming a continuous transmembrane channel in a nucleotide-free state. Here, we report its structure in an ATP-bound conformation. Large structural changes within the nucleotide-binding and transmembrane regions push conserved hydrophobic residues at the substrate entry site towards the periplasm and provide a model for polysaccharide translocation. With ATP bound, the transporter forms a large transmembrane channel with openings toward the membrane and periplasm. The channel's periplasmic exit is sealed by detergent molecules that block solvent permeation. Molecular dynamics simulation data suggest that, in a biological membrane, lipid molecules occupy this periplasmic exit and prevent water flux in the transporter's resting state.
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